This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4ba0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:4ba0.png|left|200px]]
+
==Crystal Structure of Agd31B, alpha-transglucosylase, complexed with 5F-alpha-GlcF==
 +
<StructureSection load='4ba0' size='340' side='right' caption='[[4ba0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[4ba0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BA0 FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5GF:5-FLUORO-BETA-D-GLUCOPYRANOSE'>5GF</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b9y|4b9y]], [[4b9z|4b9z]]</td></tr>
 +
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </span></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ba0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ba0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ba0 PDBsum]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The metabolism of the storage polysaccharides glycogen and starch are of vital importance to organisms from all domains of life. In bacteria, utilization of these alpha-glucans requires the concerted action of a variety of enzymes, including glycoside hydrolases, glycoside phosphorylases, and transglycosylases. In particular, transglycosylases from glycoside hydrolase families GH13 and GH77 play well-established roles in alpha-glucan sidechain (de)branching, regulation of oligo- and polysaccharide chain length, and formation of cyclic dextrans. Here, we present the biochemical and tertiary structural characterization of a new type of bacterial 1,4-alpha-glucan 4-alpha-glucosyltransferase from glycoside hydrolase family 31 (GH31). Distinct from 1,4-alpha-glucan 6-alpha-glucosyltransferases (EC 2.4.1.24) and 4-alpha-glucanotransferases (EC 2.4.1.25), this enzyme strictly transferred one glucosyl residue from alpha(1 --&gt;4) glucans in disproportionation reactions. Substrate hydrolysis was undetectable for a series of malto-oligosaccharides, except maltose, for which transglycosylation nonetheless dominated across a range of substrate concentrations. Crystallographic analysis of the enzyme in apo, acarbose-complexed, and trapped 5-beta-fluoroglucosyl-enzyme intermediate forms revealed extended substrate interactions across one negative and up to three positive subsites, thus providing structural rationalization for the unique, single-monosaccharide transferase activity of the enzyme.
-
{{STRUCTURE_4ba0| PDB=4ba0 | SCENE= }}
+
Structural enzymology of Cellvibrio japonicus Agd31B reveals alpha-transglucosylase activity in glycoside hydrolase family 31.,Larsbrink J, Izumi A, Hemsworth GR, Davies GJ, Brumer H J Biol Chem. 2012 Nov 6. PMID:23132856<ref>PMID:23132856</ref>
-
===Crystal Structure of Agd31B, alpha-transglucosylase, complexed with 5F-alpha-GlcF===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
{{ABSTRACT_PUBMED_23132856}}
+
== References ==
-
 
+
<references/>
-
==About this Structure==
+
__TOC__
-
[[4ba0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BA0 OCA].
+
</StructureSection>
[[Category: Alpha-glucosidase]]
[[Category: Alpha-glucosidase]]
[[Category: Cellvibrio japonicus]]
[[Category: Cellvibrio japonicus]]
-
[[Category: Brumer, H.]]
+
[[Category: Brumer, H]]
-
[[Category: Davies, G J.]]
+
[[Category: Davies, G J]]
-
[[Category: Hemsworth, G R.]]
+
[[Category: Hemsworth, G R]]
-
[[Category: Izumi, A.]]
+
[[Category: Izumi, A]]
-
[[Category: Larsbrink, J.]]
+
[[Category: Larsbrink, J]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]

Revision as of 17:17, 9 December 2014

Crystal Structure of Agd31B, alpha-transglucosylase, complexed with 5F-alpha-GlcF

4ba0, resolution 1.85Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ba0"
Personal tools